ID GSTP_ONCVO Reviewed; 208 AA. AC P46427; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Glutathione S-transferase 2; DE EC=2.5.1.18; DE AltName: Full=GST class-pi; GN Name=GST2; OS Onchocerca volvulus. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca. OX NCBI_TaxID=6282; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Guatemala; RX PubMed=7984170; DOI=10.1016/0166-6851(94)90030-2; RA Salinas G., Braun G., Taylor D.W.; RT "Molecular characterisation and localisation of an Onchocerca volvulus pi- RT class glutathione S-transferase."; RL Mol. Biochem. Parasitol. 66:1-9(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8050528; DOI=10.1006/expr.1994.1062; RA Liebau E., Walter R.D., Henkle-Duehrsen K.; RT "Onchocerca volvulus: isolation and sequence of a second glutathione S- RT transferase cDNA."; RL Exp. Parasitol. 79:68-71(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE, AND RP SUBUNIT. RX PubMed=15640152; DOI=10.1074/jbc.m413551200; RA Perbandt M., Hoppner J., Betzel C., Walter R.D., Liebau E.; RT "Structure of the major cytosolic glutathione S-transferase from the RT parasitic nematode Onchocerca volvulus."; RL J. Biol. Chem. 280:12630-12636(2005). CC -!- FUNCTION: Appears to play a central role in the parasite detoxification CC system. CC -!- CATALYTIC ACTIVITY: CC Reaction=glutathione + RX = a halide anion + an S-substituted CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, CC ChEBI:CHEBI:90779; EC=2.5.1.18; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15640152}. CC -!- TISSUE SPECIFICITY: Hypodermis, wall of the seminal receptacle and CC spermatozoa of adult worms. CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L28771; AAA53575.1; -; mRNA. DR EMBL; X77393; CAA54568.1; -; mRNA. DR PIR; S41933; S41933. DR PDB; 1TU7; X-ray; 1.50 A; A/B=1-208. DR PDB; 1TU8; X-ray; 1.80 A; A/B/C/D=1-208. DR PDBsum; 1TU7; -. DR PDBsum; 1TU8; -. DR AlphaFoldDB; P46427; -. DR SMR; P46427; -. DR STRING; 6282.P46427; -. DR HOGENOM; CLU_039475_2_1_1; -. DR BRENDA; 2.5.1.18; 4401. DR EvolutionaryTrace; P46427; -. DR Proteomes; UP000024404; Unassembled WGS sequence. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR CDD; cd03210; GST_C_Pi; 1. DR CDD; cd03076; GST_N_Pi; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR003082; GST_pi. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF141; GLUTATHIONE S-TRANSFERASE P; 1. DR Pfam; PF14497; GST_C_3; 1. DR Pfam; PF02798; GST_N; 1. DR PRINTS; PR01268; GSTRNSFRASEP. DR SFLD; SFLDG01205; AMPS.1; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Reference proteome; Transferase. FT CHAIN 1..208 FT /note="Glutathione S-transferase 2" FT /id="PRO_0000185914" FT DOMAIN 1..78 FT /note="GST N-terminal" FT DOMAIN 80..200 FT /note="GST C-terminal" FT BINDING 7 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000305|PubMed:15640152" FT BINDING 42 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:P09211" FT BINDING 49..50 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000305|PubMed:15640152" FT BINDING 62..63 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000305|PubMed:15640152" FT STRAND 3..11 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 15..23 FT /evidence="ECO:0007829|PDB:1TU7" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:1TU7" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:1TU7" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:1TU7" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 63..73 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 81..107 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 109..119 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:1TU7" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:1TU7" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:1TU7" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 149..164 FT /evidence="ECO:0007829|PDB:1TU7" FT TURN 166..171 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 173..183 FT /evidence="ECO:0007829|PDB:1TU7" FT HELIX 186..197 FT /evidence="ECO:0007829|PDB:1TU7" SQ SEQUENCE 208 AA; 24232 MW; D3A76450AE7A1321 CRC64; MSYKLTYFSI RGLAEPIRLF LVDQDIKFID DRIAKDDFSS IKSQFQFGQL PCLYDGDQQI VQSGAILRHL ARKYNLNGEN EMETTYIDMF CEGVRDLHVK YTRMIYMAYE TEKDPYIKSI LPGELAKFEK LLATRGNGRN LILGDKISYA DYALFEELDV HQILDPHCLD KFPLLKAFHQ RMKDRPKLKE YCEKRDAAKV PVNGNGKQ //